Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da Universidade Federal do Ceará (UFC) |
Texto Completo: | http://www.repositorio.ufc.br/handle/riufc/63573 |
Resumo: | A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms. |
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Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potentialSea hareLectinGalacturonic acidBiofilmMass spectrometryA new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms.Marine Biotechnology2022-01-18T19:54:37Z2022-01-18T19:54:37Z2017info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfCARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017.http://www.repositorio.ufc.br/handle/riufc/63573Carneiro, Rômulo FariasTorres, Renato Cézar FariasChaves, Renata PinheiroVasconcelos, Mayron Alves deSousa, Bruno Lopes deGoveia, André Castelo RodriguesArruda, Francisco VassiliepeMatos, Maria Nágila CarneiroMatthews-Cascon, HelenaFreire, Valder NogueiraTeixeira, Edson HolandaNagano, Celso ShinitiSampaio, Alexandre Holandainfo:eu-repo/semantics/openAccessporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFC2023-10-10T19:34:27Zoai:repositorio.ufc.br:riufc/63573Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:29:42.908626Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false |
dc.title.none.fl_str_mv |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
title |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
spellingShingle |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential Carneiro, Rômulo Farias Sea hare Lectin Galacturonic acid Biofilm Mass spectrometry |
title_short |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
title_full |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
title_fullStr |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
title_full_unstemmed |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
title_sort |
Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential |
author |
Carneiro, Rômulo Farias |
author_facet |
Carneiro, Rômulo Farias Torres, Renato Cézar Farias Chaves, Renata Pinheiro Vasconcelos, Mayron Alves de Sousa, Bruno Lopes de Goveia, André Castelo Rodrigues Arruda, Francisco Vassiliepe Matos, Maria Nágila Carneiro Matthews-Cascon, Helena Freire, Valder Nogueira Teixeira, Edson Holanda Nagano, Celso Shiniti Sampaio, Alexandre Holanda |
author_role |
author |
author2 |
Torres, Renato Cézar Farias Chaves, Renata Pinheiro Vasconcelos, Mayron Alves de Sousa, Bruno Lopes de Goveia, André Castelo Rodrigues Arruda, Francisco Vassiliepe Matos, Maria Nágila Carneiro Matthews-Cascon, Helena Freire, Valder Nogueira Teixeira, Edson Holanda Nagano, Celso Shiniti Sampaio, Alexandre Holanda |
author2_role |
author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Carneiro, Rômulo Farias Torres, Renato Cézar Farias Chaves, Renata Pinheiro Vasconcelos, Mayron Alves de Sousa, Bruno Lopes de Goveia, André Castelo Rodrigues Arruda, Francisco Vassiliepe Matos, Maria Nágila Carneiro Matthews-Cascon, Helena Freire, Valder Nogueira Teixeira, Edson Holanda Nagano, Celso Shiniti Sampaio, Alexandre Holanda |
dc.subject.por.fl_str_mv |
Sea hare Lectin Galacturonic acid Biofilm Mass spectrometry |
topic |
Sea hare Lectin Galacturonic acid Biofilm Mass spectrometry |
description |
A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017 2022-01-18T19:54:37Z 2022-01-18T19:54:37Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
CARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017. http://www.repositorio.ufc.br/handle/riufc/63573 |
identifier_str_mv |
CARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017. |
url |
http://www.repositorio.ufc.br/handle/riufc/63573 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Marine Biotechnology |
publisher.none.fl_str_mv |
Marine Biotechnology |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da Universidade Federal do Ceará (UFC) instname:Universidade Federal do Ceará (UFC) instacron:UFC |
instname_str |
Universidade Federal do Ceará (UFC) |
instacron_str |
UFC |
institution |
UFC |
reponame_str |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
collection |
Repositório Institucional da Universidade Federal do Ceará (UFC) |
repository.name.fl_str_mv |
Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC) |
repository.mail.fl_str_mv |
bu@ufc.br || repositorio@ufc.br |
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1813028827924791296 |